KCNN1_MOUSE
ID KCNN1_MOUSE Reviewed; 537 AA.
AC Q9EQR3; Q5CZY7; Q6JXY1; Q99JA9;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 159.
DE RecName: Full=Small conductance calcium-activated potassium channel protein 1;
DE Short=SK1;
DE Short=SKCa 1;
DE Short=SKCa1;
DE AltName: Full=KCa2.1;
GN Name=Kcnn1; Synonyms=Sk1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP [MRNA] OF 1-131 (ISOFORM 1), ALTERNATIVE SPLICING, INTERACTION WITH
RP CALMODULIN, AND POLYMORPHISM OF POLY-GLU REGION.
RC STRAIN=CD-1;
RX PubMed=11267657; DOI=10.1016/s0167-4781(01)00166-x;
RA Shmukler B.E., Bond C.T., Wilhelm S., Bruening-Wright A., Maylie J.,
RA Adelman J.P., Alper S.L.;
RT "Structure and complex transcription pattern of the mouse SK1 KCa channel
RT gene, KCNN1.";
RL Biochim. Biophys. Acta 1518:36-46(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Colon;
RX PubMed=11557517; DOI=10.1152/ajpgi.2001.281.4.g964;
RA Ro S., Hatton W.J., Koh S.D., Horowitz B.;
RT "Molecular properties of small-conductance Ca2+-activated K+ channels
RT expressed in murine colonic smooth muscle.";
RL Am. J. Physiol. 281:G964-G973(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=CD-1; TISSUE=Heart;
RX PubMed=16055520; DOI=10.1152/ajpheart.00534.2005;
RA Tuteja D., Xu D., Timofeyev V., Lu L., Sharma D., Zhang Z., Xu Y., Nie L.,
RA Vazquez A.E., Young J.N., Glatter K.A., Chiamvimonvat N.;
RT "Differential expression of small-conductance Ca2+-activated K+ channels
RT SK1, SK2, and SK3 in mouse atrial and ventricular myocytes.";
RL Am. J. Physiol. 289:H2714-H2723(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS GLU-66 INS
RP AND GLN-522.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Forms a voltage-independent potassium channel activated by
CC intracellular calcium (PubMed:11557517). Activation is followed by
CC membrane hyperpolarization (PubMed:11557517). Thought to regulate
CC neuronal excitability by contributing to the slow component of synaptic
CC afterhyperpolarization (PubMed:11557517).
CC {ECO:0000269|PubMed:11557517}.
CC -!- ACTIVITY REGULATION: Inhibited by bee venom neurotoxin apamin.
CC Inhibited by d-tubocurarine and tetraethylammonium (TEA).
CC {ECO:0000250|UniProtKB:Q92952}.
CC -!- SUBUNIT: Heterooligomer. The complex is composed of 4 channel subunits
CC each of which binds to a calmodulin subunit which regulates the channel
CC activity through calcium-binding (By similarity). Interacts with
CC calmodulin. {ECO:0000250, ECO:0000269|PubMed:11267657}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Comment=At least 16 isoforms may be produced by combinatorial
CC splicing of the N-terminal exon 3.1 and the C-terminal exons 7, 8a
CC and 9. Experimental confirmation may be lacking for some isoforms.;
CC Name=1;
CC IsoId=Q9EQR3-1; Sequence=Displayed;
CC Name=2; Synonyms=I;
CC IsoId=Q9EQR3-2; Sequence=VSP_002809;
CC Name=3; Synonyms=V;
CC IsoId=Q9EQR3-3; Sequence=VSP_002810;
CC Name=4; Synonyms=VI;
CC IsoId=Q9EQR3-4; Sequence=VSP_002810, VSP_002813;
CC Name=5; Synonyms=VII;
CC IsoId=Q9EQR3-5; Sequence=VSP_002810, VSP_002811;
CC Name=6; Synonyms=VIII;
CC IsoId=Q9EQR3-6; Sequence=VSP_002810, VSP_002812;
CC Name=7; Synonyms=IV;
CC IsoId=Q9EQR3-7; Sequence=VSP_002812;
CC Name=8; Synonyms=III;
CC IsoId=Q9EQR3-8; Sequence=VSP_002811;
CC Name=9; Synonyms=II;
CC IsoId=Q9EQR3-9; Sequence=VSP_002813;
CC -!- TISSUE SPECIFICITY: Highest expression in brain and liver with lower
CC levels in heart, testis, kidney and colon. In colon, detected in smooth
CC muscle cells. Expressed in atrial and ventricular myocytes with higher
CC levels in atrial myocytes. {ECO:0000269|PubMed:11557517,
CC ECO:0000269|PubMed:16055520}.
CC -!- POLYMORPHISM: The poly-Glu region of KCNN1 is polymorphic and the
CC number of Glu varies between strains (from 10 to 12). The repeat with
CC 10 Glu residues (shown here) is found in BALB/c, DBA/2J, 129/SvJ, A/J,
CC C3H/HeJ, BALB/cJ, BXD-31, SM/J, ST/BJ, FVB/NJ, NZB/B1NJ, CBA/J and
CC CAST/Ei. {ECO:0000269|PubMed:11267657}.
CC -!- MISCELLANEOUS: [Isoform 1]: Produced by alternative splicing events in
CC which various combinations of the four 5' non-coding exons A, B1, B2 or
CC C are joined directly to exon 3.2.
CC -!- MISCELLANEOUS: [Isoform 3]: Reduced calmodulin-binding. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Reduced calmodulin-binding. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: Reduced calmodulin-binding. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 6]: Reduced calmodulin-binding. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 7]: Reduced calmodulin-binding. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 8]: Reduced calmodulin-binding. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the potassium channel KCNN family. KCa2.1/KCNN1
CC subfamily. {ECO:0000305}.
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DR EMBL; AF116525; AAG43216.1; -; mRNA.
DR EMBL; AF297870; AAK30363.1; -; Genomic_DNA.
DR EMBL; AF297869; AAK30363.1; JOINED; Genomic_DNA.
DR EMBL; AF303461; AAK29550.1; -; mRNA.
DR EMBL; AF303462; AAK29551.1; -; mRNA.
DR EMBL; AF303463; AAK29552.1; -; mRNA.
DR EMBL; AF357239; AAK48900.1; -; mRNA.
DR EMBL; AY258143; AAP45948.1; -; mRNA.
DR EMBL; BC090622; AAH90622.1; -; mRNA.
DR RefSeq; NP_115773.2; NM_032397.2.
DR RefSeq; XP_006509870.1; XM_006509807.3.
DR RefSeq; XP_006509871.1; XM_006509808.3.
DR AlphaFoldDB; Q9EQR3; -.
DR SMR; Q9EQR3; -.
DR BioGRID; 219999; 1.
DR STRING; 10090.ENSMUSP00000105708; -.
DR TCDB; 9.A.48.1.1; the unconventional protein secretion (ups) system.
DR PhosphoSitePlus; Q9EQR3; -.
DR MaxQB; Q9EQR3; -.
DR PaxDb; Q9EQR3; -.
DR PeptideAtlas; Q9EQR3; -.
DR PRIDE; Q9EQR3; -.
DR ProteomicsDB; 269274; -. [Q9EQR3-1]
DR ProteomicsDB; 269275; -. [Q9EQR3-2]
DR ProteomicsDB; 269276; -. [Q9EQR3-3]
DR ProteomicsDB; 269277; -. [Q9EQR3-4]
DR ProteomicsDB; 269278; -. [Q9EQR3-5]
DR ProteomicsDB; 269279; -. [Q9EQR3-6]
DR ProteomicsDB; 269280; -. [Q9EQR3-7]
DR ProteomicsDB; 269281; -. [Q9EQR3-8]
DR ProteomicsDB; 269282; -. [Q9EQR3-9]
DR DNASU; 84036; -.
DR GeneID; 84036; -.
DR KEGG; mmu:84036; -.
DR UCSC; uc012gfj.1; mouse. [Q9EQR3-2]
DR CTD; 3780; -.
DR MGI; MGI:1933993; Kcnn1.
DR eggNOG; KOG3684; Eukaryota.
DR InParanoid; Q9EQR3; -.
DR OrthoDB; 907751at2759; -.
DR PhylomeDB; Q9EQR3; -.
DR Reactome; R-MMU-1296052; Ca2+ activated K+ channels.
DR BioGRID-ORCS; 84036; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Kcnn1; mouse.
DR PRO; PR:Q9EQR3; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9EQR3; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005516; F:calmodulin binding; IDA:MGI.
DR GO; GO:0005242; F:inward rectifier potassium channel activity; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0016286; F:small conductance calcium-activated potassium channel activity; ISO:MGI.
DR GO; GO:0006811; P:ion transport; IBA:GO_Central.
DR GO; GO:0071805; P:potassium ion transmembrane transport; ISO:MGI.
DR InterPro; IPR004178; CaM-bd_dom.
DR InterPro; IPR036122; CaM-bd_dom_sf.
DR InterPro; IPR015449; K_chnl_Ca-activ_SK.
DR InterPro; IPR013099; K_chnl_dom.
DR PANTHER; PTHR10153; PTHR10153; 1.
DR Pfam; PF02888; CaMBD; 1.
DR Pfam; PF07885; Ion_trans_2; 1.
DR Pfam; PF03530; SK_channel; 1.
DR PRINTS; PR01451; SKCHANNEL.
DR SMART; SM01053; CaMBD; 1.
DR SUPFAM; SSF81327; SSF81327; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calmodulin-binding; Ion channel; Ion transport;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..537
FT /note="Small conductance calcium-activated potassium
FT channel protein 1"
FT /id="PRO_0000155008"
FT TRANSMEM 108..128
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT INTRAMEM 314..334
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..363
FT /note="Segment S6"
FT /evidence="ECO:0000255"
FT REGION 381..460
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1
FT /note="M -> MFWNGQGDVQPLLSPQVHSEALLRNHAGPQRACCTPSPRRQVAM
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11267657"
FT /id="VSP_002809"
FT VAR_SEQ 351..387
FT /note="Missing (in isoform 3, isoform 4, isoform 5 and
FT isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_002810"
FT VAR_SEQ 423..537
FT /note="KFLQAIHQAQKLRSVKIEQGKVNDQANTLAELAKAQSIAYEVVSELQAQQEE
FT LEARLAALESRLDVLGASLQALPGLIAQAICPLPPPWPGPGHLATATHSPQSHWLPTMG
FT SDCG -> LRSSEV (in isoform 5 and isoform 8)"
FT /evidence="ECO:0000305"
FT /id="VSP_002811"
FT VAR_SEQ 423..537
FT /note="KFLQAIHQAQKLRSVKIEQGKVNDQANTLAELAKAQSIAYEVVSELQAQQEE
FT LEARLAALESRLDVLGASLQALPGLIAQAICPLPPPWPGPGHLATATHSPQSHWLPTMG
FT SDCG -> SEV (in isoform 6 and isoform 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_002812"
FT VAR_SEQ 431..433
FT /note="Missing (in isoform 4 and isoform 9)"
FT /evidence="ECO:0000305"
FT /id="VSP_002813"
FT VARIANT 66
FT /note="E -> EE (in strain: C57BL/6J, A/HeJ and SPRET/Ei)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT VARIANT 66
FT /note="E -> EEE (in strain: SWR/J, AKR/J, RBF/DNJ and P/J)"
FT VARIANT 522
FT /note="H -> Q (in strain: C57BL/6J)"
FT /evidence="ECO:0000269|PubMed:15489334"
SQ SEQUENCE 537 AA; 59330 MW; F3DCFCB9FF309A4F CRC64;
MSSHSHNGSV GQPLGSGPGF LGWEPVDPEA GRPLQPTQGP GLQMVAKGQP VRLSPGGSRG
HPQEQEEEEE EEEEEDKTGS GKPPTVSHRL GHRRALFEKR KRLSDYALIF GMFGIVVMVT
ETELSWGVYT KESLCSFALK CLISLSTVIL LGLVILYHAR EIQLFLVDNG ADDWRIAMTW
ERVSLISLEL VVCAIHPVPG HYRFTWTARL AFSLVPSAAE ADLDVLLSIP MFLRLYLLAR
VMLLHSRIFT DASSRSIGAL NRVTFNTRFV TKTLMTICPG TVLLVFSVSS WIVAAWTVRV
CERYHDKQEV TSNFLGAMWL ISITFLSIGY GDMVPHTYCG KGVCLLTGIM GAGCTALVVA
VVARKLELTK AEKHVHNFMM DTQLTKRVKN AAANVLRETW LIYKHTRLVK KPDQGRVRKH
QRKFLQAIHQ AQKLRSVKIE QGKVNDQANT LAELAKAQSI AYEVVSELQA QQEELEARLA
ALESRLDVLG ASLQALPGLI AQAICPLPPP WPGPGHLATA THSPQSHWLP TMGSDCG
